ID   C5P7L6_COCP7            Unreviewed;      1011 AA.
AC   C5P7L6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific {ECO:0000256|ARBA:ARBA00018028};
DE            EC=2.1.1.359 {ECO:0000256|ARBA:ARBA00012178};
DE   AltName: Full=SET domain-containing protein 2 {ECO:0000256|ARBA:ARBA00030091};
GN   ORFNames=CPC735_027520 {ECO:0000313|EMBL:EER27416.1};
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929 {ECO:0000313|EMBL:EER27416.1, ECO:0000313|Proteomes:UP000009084};
RN   [1] {ECO:0000313|EMBL:EER27416.1, ECO:0000313|Proteomes:UP000009084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: Histone methyltransferase that trimethylates histone H3 'Lys-
CC       36' forming H3K36me3. Involved in transcription elongation as well as
CC       in transcription repression. {ECO:0000256|ARBA:ARBA00003901}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC         COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC         Evidence={ECO:0000256|ARBA:ARBA00000317};
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EER27416.1}.
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DR   EMBL; ACFW01000025; EER27416.1; -; Genomic_DNA.
DR   RefSeq; XP_003069561.1; XM_003069515.1.
DR   AlphaFoldDB; C5P7L6; -.
DR   GeneID; 9695056; -.
DR   KEGG; cpw:CPC735_027520; -.
DR   VEuPathDB; FungiDB:CPC735_027520; -.
DR   HOGENOM; CLU_008492_0_1_1; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd19172; SET_SETD2; 1.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 1.10.1740.100; Set2, Rpb1 interacting domain; 1.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR025788; Set2_fungi.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR044437; SETD2/Set2_SET.
DR   InterPro; IPR013257; SRI.
DR   InterPro; IPR038190; SRI_sf.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR017923; TFIIS_N.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR22884:SF413; HISTONE-LYSINE N-METHYLTRANSFERASE CG1716-RELATED; 1.
DR   PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF08711; Med26; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF08236; SRI; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS51568; SAM_MT43_SET2_1; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          146..201
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          203..320
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          327..343
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          604..635
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          782..1011
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..697
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..872
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..925
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..950
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        983..1004
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1011 AA;  113732 MW;  858BFFAD67590DD9 CRC64;
     MAGHDDEEAR IETVKDAVTD MKLERQSSTE SIAPNGILDT ITPKDEPNGH LSSKPSTPSL
     KPPKSRSRSS NSLAKDEVPE EKVGGDITIK QEPGQPPKLA RSASQKLPAR AAPLFTDLPD
     KTTEATSTFQ LMEVCTYANK YLGYTEHAMD CDCAEEWDAA TCRNTACGED SDCINRATKM
     ECFGDCGCGD SCQNQRFQRR EYAKVSVIKT EKKGYGLRAD CDLRPNEFIF EYIGEVINEP
     QFRRRMIQYD EEGIKHFYFM SLNKGEFVDA TKKGNLGRFC NHSCNPNCYV DKWVVGEKLR
     MGIFAERYIK AGEELVFNYN VDRYGADPQP CYCGEPNCTG FIGGKTQTER ATKLSHATIE
     ALGIDDPDGW DTAVARRPRK KKTGEDDEEY VDSLQPKSLD ENGVTKVMAA LMQCKEKWIA
     VKLLGRIQRC EDERVRHRVV RMHGYQILNS QLNTWKDDFN VVLQILDILD KFPRLTRNKI
     IDSKIEGTVS PLQECDDERV AEKAKALLEI WSALEVGYRI PRMKRDPAAV NNTPTANHYE
     RRETAKDDRK PNSSKSRSSS RSRSRSVDVT RNAPRGPAAL TRGGGKGHMH SYRPGQRPFR
     RPFNPLPKGW FAAESNGRTY YYSATGETTW SRPTAPAVQP PPPPKRESKE KTLQDIIDGI
     MNAKENTPKA KDKSATPATP ADAKIPEKKE HKEKWRSYSE EKQKKLYENT LFPHVKYIVD
     KFKHKLPKDD LKRYAKEVAK KLVNSDFKNN RVEDPTKISE KQIKQVKKYC KEYFDKAVAK
     HRAYEEKKAE RKSKGSVKAT TSATIDKAET TSTKAPPQFD GAAETGDGDS DVQLSDAEYE
     DGQEGSSHHS GLKRKRTDDE DFENDHENGG VSPTKRQRSA SLPIIPPPPP PMSPSNLVLD
     DGSREALKRQ RTEGAEDDEY GDSTISSGKR QRSETPPPPP PPPPPADIPP ENIESENEND
     KDQEELQDYD VQEAKWGKED NIAIQSPSHS PFPAQSISNH SNTAHETDSH S
//